Mucin-specific bark lectin from elderberry Sambucus sieboldiana and its applications to the affinity chromatography of mucin.
Three bark lectins were isolated from elderberry Sambucus sieboldiana using fetuin-Sepharose 4B and mucin-Sepharose 4B, and were studied comparatively for their binding to glycoprotein and to clarify various physicochemical features. For each, a unique pattern on isoelectric focusing was noted and their affinity toward various glycoproteins differed, indicating the structures of their carbohydrate binding sites possibly differ. One bark lectin showed specific binding toward porcine mucin. The purity of mucin from a crude porcine stomach mucin or an extract of porcine submaxillary glands could be improved by affinity chromatography on immobilized lectin having binding specificity toward mucin.
Harada
H
H
Honen Corporation, Laboratory, Shizuoka, Japan.
Kondo
M
M
Yanagisawa
M
M
Sunada
S
S
D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D037102:Lectins / Q000302:isolation & purification* / Q000378:metabolism; D009077:Mucins / Q000302:isolation & purification*; D037121:Plant Lectins; D010944:Plants / Q000032:analysis; D011485:Protein Binding; D013552:Swine
D006023:Glycoproteins; D037102:Lectins; D009077:Mucins; D037121:Plant Lectins